The Golgi Sialoglycoprotein MG160, Expressed in Pichia pastoris, Does Not Require Complex Carbohydrates and Sialic Acid for Secretion and Basic Fibroblast Growth Factor Binding
Open Access
- 8 May 1997
- journal article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 234 (1) , 68-72
- https://doi.org/10.1006/bbrc.1997.6580
Abstract
No abstract availableKeywords
This publication has 17 references indexed in Scilit:
- Cloning and Sequence Analysis of the Human MG160, a Fibroblast Growth Factor and E-Selectin Binding Membrane Sialoglycoprotein of the Golgi ApparatusDNA and Cell Biology, 1996
- MG160, a Membrane Protein of the Golgi Apparatus Which Is Homologous to a Fibroblast Growth Factor Receptor and to a Ligand for E-selectin, Is Found Only in the Golgi Apparatus and Appears Early in Chicken Embryo DevelopmentExperimental Cell Research, 1995
- Assignment of the GLG1 Gene for MG-160, a Fibroblast Growth Factor and E-Selectin Binding Membrane Sialoglycoprotein of the Golgi Apparatus, to Chromosome 16q22-q23 by Fluorescence in Situ HybridizationGenomics, 1995
- Production of mouse epidermal growth factor in yeast: high-level secretion using Pichia pastoris strains containing multiple gene copiesGene, 1991
- Immunocytochemical visualization of the Golgi apparatus in several species, including human, and tissues with an antiserum against MG-160, a sialoglycoprotein of rat Golgi apparatus.Journal of Histochemistry & Cytochemistry, 1990
- Deglycosylation of asparagine-linked glycans by peptide:N-glycosidase FBiochemistry, 1985
- Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications.Proceedings of the National Academy of Sciences, 1979
- Transfer of purified herpes virus thymidine kinase gene to cultured mouse cellsCell, 1977
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970